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THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE
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Structural highlights
FunctionF261_RAT Synthesis and degradation of fructose 2,6-bisphosphate. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the fructose-2,6-bisphosphatase domain trapped during the reaction reveal a phosphorylated His 258, and a water molecule immobilized by the product, fructose-6-phosphate. The geometry suggests that the dephosphorylation step requires prior removal of the product for an 'associative in-line' phosphoryl transfer to the catalytic water. Crystal structure of a trapped phosphoenzyme during a catalytic reaction.,Lee YH, Olson TW, Ogata CM, Levitt DG, Banaszak LJ, Lange AJ Nat Struct Biol. 1997 Aug;4(8):615-8. PMID:9253407[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References | ||||||||||||||||||||
This page was last modified 22:15, 26 March 2025.